Anomalous diffusion and dynamical correlation between the side chains and the main chain of proteins in their native state.

ABSTRACT: Structural fluctuations of a protein are essential for a protein to function and fold. By using molecular dynamics (MD) simulations of the model α/β protein VA3 in its native state, the coupling between the main-chain (MC) motions [represented by coarse-grained dihedral angles (CGDAs) γ(n) based on four successive C(α) atoms (n - 1, n, n + 1, n + 2) along the amino acid sequence] and its side-chain (SC) motions [represented by CGDAs δ(n) formed by the virtual bond joining two consecutive C(α) atoms (n, n + 1) and the bonds joining these C(α) atoms to their respective C(β) atoms] was analyzed. The motions of SCs (δ(n)) and MC (γ(n)) over time occur on similar free-energy profiles and were found to be subdiffusive. The fluctuations of the SCs (δ(n)) and those of the MC (γ(n)) are generally p

SUBMITTER: Cote Y 

PROVIDER: S-EPMC3387131 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature